Analysis of Carboxy Terminal Domain of Metalloprotease of Elastolytic Aeromonas hydrophila
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- Takahashi Eizo
- Laboratory of Protein Function, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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- Kobayashi Hidetomo
- Laboratory of Molecular Microbiological Science, Faculty of Pharmaceutical Sciences, Hiroshima International University
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- Yamanaka Hiroyasu
- Laboratory of Molecular Microbiological Science, Faculty of Pharmaceutical Sciences, Hiroshima International University
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- Nakanishi Mayu
- Laboratory of Protein Function, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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- Tateishi Arisa
- Laboratory of Protein Function, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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- Abe Takemi
- Laboratory of Protein Function, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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- Arimoto Sakae
- Laboratory of Protein Function, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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- Negishi Tomoe
- Laboratory of Protein Function, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
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- Okamoto Keinosuke
- Laboratory of Protein Function, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
書誌事項
- タイトル別名
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- Analysis of Carboxy Terminal Domain of Metalloprotease of Elastolytic <i>Aeromonas hydrophila</i>
- Analysis of carboxy terminal domain of metalloprotease of elastolytic <italic>Aeromonas hydrophila</italic>
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抄録
We examined the ability of Aeromonas hydrophila to lyse elastin. Eight of 13 strains showed elastolytic activity on agar medium containing elastin and 5 strains did not. In order to examine the involvement of the metalloprotease of A. hydrophila (AMP) in elastolytic activity, we made the amp-deletion mutant strain from an elastolytic strain. The elastolytic activity of the strain decreased with this deletion. The analysis of AMP released into the culture supernatant showed that AMP appeared outside of the cell as the intermediate consisting of a mature domain and carboxy terminal (C-terminal) propeptide domain. Further analysis showed that the intermediate has the ability to lyse elastin and that loss of the C-terminal domain causes loss of the elastolytic activity of the intermediate. We then determined the nucleotide sequence of the amps of all strains used in this study. Phylogenetic analysis revealed that these AMPs were divided into three groups. The AMPs from elastolytic strains belong to group I or group II, and AMPs from non-elastolytic strains belong to group III. The distance between group I and group II is small, but group III is located separately from groups I and II. Comparison of the amino acid residues of the C-terminal domain revealed that there are 13 amino acid residues specific to the C-terminal domain of group III. This indicates that the conformation of the C-terminal propeptide domain formed by these specific amino acid residues is important for AMP to express elastolytic activity.
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 36 (7), 1174-1182, 2013
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390282679609271424
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- NII論文ID
- 130003361477
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- NII書誌ID
- AA10885497
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- COI
- 1:STN:280:DC%2BC3sjmsVKlsQ%3D%3D
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 024644732
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- PubMed
- 23811566
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可